ID   BGLF_ASPFN              Reviewed;         866 AA.
AC   B8NP65;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Probable beta-glucosidase F;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase F;
DE   AltName: Full=Cellobiase F;
DE   AltName: Full=Gentiobiase F;
DE   Flags: Precursor;
GN   Name=bglF; ORFNames=AFLA_128480;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC   SRRC 167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
CC   -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes
CC       involved in the degradation of cellulosic biomass. Catalyzes the last
CC       step releasing glucose from the inhibitory cellobiose (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; EQ963481; EED48625.1; -; Genomic_DNA.
DR   RefSeq; XP_002382041.1; XM_002382000.1.
DR   AlphaFoldDB; B8NP65; -.
DR   SMR; B8NP65; -.
DR   STRING; 332952.B8NP65; -.
DR   GlyCosmos; B8NP65; 11 sites, No reported glycans.
DR   EnsemblFungi; EED48625; EED48625; AFLA_128480.
DR   VEuPathDB; FungiDB:AFLA_012667; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_2_0_1; -.
DR   OMA; PAPYGGW; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..866
FT                   /note="Probable beta-glucosidase F"
FT                   /id="PRO_0000394110"
FT   REGION          725..748
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        285
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        328
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        360
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        395
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        421
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        474
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        659
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        664
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        724
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   866 AA;  93066 MW;  02697819B5DDB341 CRC64;
     MAAFPAYLAL LSYLVPGALS HPEAKTLTSR ASTEAYSPPY YPAPNGGWIS EWASAYEKAH
     RVVSNMTLAE KVNLTSGTGI YMGPCAGQTG SVPRFGIPNL CLHDSPLGVR NSDHNTAFPA
     GITVGATFDK DLMYERGVGL GEEARGKGIN VLLGPSVGPI GRKPRGGRNW EGFGADPSLQ
     AFGGSLTIKG MQSTGAIASL KHLIGNEQEQ HRMSSVITQG YSSNIDDRTL HELYLWPFAE
     SVRAGAGSVM IAYNDVNRSA CSQNSKLING ILKDELGFQG FVVTDWLAHI GGVSSALAGL
     DMSMPGDGAI PLLGTSYWSW ELSRSVLNGS VPVERLNDMV TRIVATWYKM GQDKDYPLPN
     FSSNTEDETG PLYPGALFSP SGIVNQYVNV QGNHNVTARA IARDAITLLK NNDNVLPLKR
     NNTLKIFGTD AGTNSDGINS CTDKGCNKGV LTMGWGSGTS RLPYLITPQE AIANISSNAG
     FHITDTFPSG VTAGPDDIAI VFINSDSGEN YITVDGNPGD RTLAGLHAWH NGDNLVKAAA
     EKFSNVVVVV HTVGPILMEE WIDLDSVKAV LVAHLPGQEA GWSLTDILFG DYSPSGHLPY
     TIPHSESDYP ESVGLIAQPF GQIQDDYTEG LYIDYRHFLK ANITPRYPFG HGLSYTTFNF
     TEPNLSIIKA LDTAYPAARP PKGSTPTYPT AKPDASEVAW PKNFNRIWRY LYPYLDNPEG
     AAANSSKTYP YPDGYTTEPK PAPRAGGAEG GNPALWDVTF SVQVKVTNTG SRDGRAVAQL
     YVELPSSLGL DTPSRQLRQF EKTKILAAGE SEVLTLDVTR KDLSVWDVVV QDWKAPVNGE
     GVKIWVGESV ADLRVGCVVG EGCSTL
//